Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification and mechanism of action of two histidine residues underlying high-affinity Zn2+ inhibition of the NMDA receptor.

Neuron - 1 May 1999

Choi Y B, Lipton S A

Abstract excerpt

Zinc (Zn2+) inhibition of N-methyl-D-aspartate receptor (NMDAR) activity involves both voltage-independent and voltage-dependent components. Recombinant NR1/NR2A and NR1/NR2B receptors exhibit similar voltage-dependent block, but voltage-independent Zn2+ inhibition occurs with much higher affinity for NR1/NR2A than NR1/NR2B receptors (nanomolar versus micromolar IC50, respectively). Here, we show that two...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Histidine
Share to Mutation
Share to Oocytes

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Patch-Clamp Techniques

Share to Protein Isoforms

Share to Receptors, N-Methyl-D-Aspartate

Share to Xenopus laevis

Source

Identifiers

PMID: 10402203
DOI: 10.1016/s0896-6273(00)80763-1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and mechanism of action of two histidine residues underlying high-affinity Zn2+ inhibition of the NMDA receptor.PMID 10402203Read ↗

Control of voltage-independent zinc inhibition of NMDA receptors by the NR1 subunit.Semantic proximity Read ↗

The micromolar zinc-binding domain on the NMDA receptor subunit NR2B.Semantic proximity Read ↗

Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor.Semantic proximity Read ↗

Activity Dependent Inhibition of AMPA Receptors by Zn2.Semantic proximity Read ↗

Zinc alleviates pain through high-affinity binding to the NMDA receptor NR2A subunit.Semantic proximity Read ↗

Subunit-dependent high-affinity zinc inhibition of acid-sensing ion channels.Semantic proximity Read ↗

Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.Semantic proximity Read ↗

Adjacent asparagines in the NR2-subunit of the NMDA receptor channel control the voltage-dependent block by extracellular Mg2+.Semantic proximity Read ↗

Intracellular Mg2+ interacts with structural determinants of the narrow constriction contributed by the NR1-subunit in the NMDA receptor channel.Semantic proximity Read ↗

Supralinear potentiation of NR1/NR3A excitatory glycine receptors by Zn2+ and NR1 antagonist.Semantic proximity Read ↗

Molecular and functional diversity of the NMDA receptor channel.Semantic proximity Read ↗

Site within N-Methyl-D-aspartate receptor pore modulates channel gating.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.